LCL3_ASPFN
ID LCL3_ASPFN Reviewed; 277 AA.
AC B8MY73;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Probable endonuclease lcl3;
DE EC=3.1.-.-;
GN Name=lcl3; ORFNames=AFLA_080100;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000250}; Single-
CC pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LCL3 family. {ECO:0000305}.
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DR EMBL; EQ963472; EED57315.1; -; Genomic_DNA.
DR RefSeq; XP_002372927.1; XM_002372886.1.
DR AlphaFoldDB; B8MY73; -.
DR SMR; B8MY73; -.
DR STRING; 5059.CADAFLAP00000792; -.
DR EnsemblFungi; EED57315; EED57315; AFLA_080100.
DR VEuPathDB; FungiDB:AFLA_080100; -.
DR eggNOG; ENOG502RZZQ; Eukaryota.
DR HOGENOM; CLU_046484_0_1_1; -.
DR OMA; IYHTPGG; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR Pfam; PF00565; SNase; 1.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 3: Inferred from homology;
KW Calcium; Endonuclease; Hydrolase; Membrane; Metal-binding; Mitochondrion;
KW Nuclease; Transmembrane; Transmembrane helix.
FT CHAIN 1..277
FT /note="Probable endonuclease lcl3"
FT /id="PRO_0000408644"
FT TRANSMEM 42..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 80..248
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
SQ SEQUENCE 277 AA; 32129 MW; C051A4A1EEDEC79A CRC64;
MRWPPWASES QARDKQDEQN QKNWDKSLNA IDWAAFTEPR TLIPTLILTT GIIGALQIHR
RYLRRFPDAV SISPSYFRKR TILGQVTSVG DGDGFRLYHT PGGRLAGWGW LPWKRVPTAK
KDLRDKTISV RLAGVDAPEL AHFGRPEQPY AREAHEWLTS YVLNRRVRVL VHRQDQYQRV
VASAYVRRAI DFPIPFRRRD VSYEMLTRGL ATVYEAKAGS EFGGPELERK YREAESIAKR
KGTGLWKGYR RNRKGWESPR EYKTRMGLEE QSQGKGN
